Mutational Analysis of Intrinsic Regions of Presenilin 2 That Determine Its Endoproteolytic Cleavage and Pathological Function
Open Access
- 1 February 2000
- journal article
- Published by Elsevier
- Vol. 275 (5), 3681-3686
- https://doi.org/10.1074/jbc.275.5.3681
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Additive Effects of PS1 and APP Mutations on Secretion of the 42-Residue Amyloid β-ProteinNeurobiology of Disease, 1998
- Both N-terminal and C-terminal fragments of Presenilin 1 colocalize with neurofibrillary tangles in neurons and dystrophic neurites of senile plaques in Alzheimer's diseaseJournal of Neuroscience Research, 1998
- The Presenilin 1 Protein Is a Component of a High Molecular Weight Intracellular Complex That Contains β-CateninJournal of Biological Chemistry, 1998
- Alzheimer's Disease Associated Presenilin-1 Holoprotein and Its 18−20 kDa C-Terminal Fragment Are Death Substrates for Proteases of the Caspase FamilyBiochemistry, 1998
- Determination of a Cleavage Site of Presenilin 2 Protein in Stably Transfected SH-SY5Y Human Neuroblastoma Cell LinesBiochemical and Biophysical Research Communications, 1997
- Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In VivoNeuron, 1996
- Characterization of human presenilin 1 using N‐terminal specific monoclonal antibodies: Evidence that Alzheimer mutations affect proteolytic processingFEBS Letters, 1996
- A mutation in Alzheimerʼs disease destroying a splice acceptor site in the presenilin-1 geneNeuroReport, 1995
- Facilitation of lin-12-mediated signalling by sel-12, a Caenorhabditis elegans S182 Alzheimer's disease geneNature, 1995
- Formation of amyloid-like fibrils in COS cells overexpressing part of the Alzheimer amyloid protein precursorNature, 1990